ID A0A2G5HLW3_CERBT Unreviewed; 677 AA.
AC A0A2G5HLW3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Palmitoyltransferase PFA4 {ECO:0000256|HAMAP-Rule:MF_03199};
DE EC=2.3.1.225 {ECO:0000256|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein S-acyltransferase {ECO:0000256|HAMAP-Rule:MF_03199};
DE Short=PAT {ECO:0000256|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein fatty acyltransferase 4 {ECO:0000256|HAMAP-Rule:MF_03199};
GN Name=PFA4 {ECO:0000256|HAMAP-Rule:MF_03199};
GN ORFNames=CB0940_04258 {ECO:0000313|EMBL:PIA93498.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA93498.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA93498.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA93498.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC proteins, thereby regulating their membrane association and biological
CC function. {ECO:0000256|HAMAP-Rule:MF_03199}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000256|ARBA:ARBA00001870,
CC ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03199}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03199}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIA93498.1}.
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DR EMBL; LKMD01000105; PIA93498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HLW3; -.
DR OrthoDB; 6683at2759; -.
DR Proteomes; UP000230605; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR InterPro; IPR015418; Eaf6.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR033682; PFA4.
DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF19; S-ACYLTRANSFERASE; 1.
DR Pfam; PF01529; DHHC; 1.
DR Pfam; PF09340; NuA4; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119}; Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_03199};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 45..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 146..169
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 181..206
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT DOMAIN 96..224
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 369..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 517..551
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 388..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199"
SQ SEQUENCE 677 AA; 76803 MW; D79B54C2C2DAA77A CRC64;
MELKDLPLVQ RLALPAVSSL IAFLAYTSQW LFHRIEPGPL SSGEAYIFNA LVACIFICYW
RTCLTDPGTI PKDWHESLSG QESNAKQTAT KAAAQSNRWC RRCEAFKPPR AHHCKTCKRC
IMKMDHHCVW TANCVSHITI PHFIRFLFYA VASMSFLEYF LFLRVAPIWA KRSLPRYLGP
FVLQLSHIFV LFAVNSFVLF ALTLLLGRTL WSLAVNTWTI EGWEIERHDA VLRRARVLGG
YLEDPDGNKI FIEHQEFPWD IGIWANICQG MGSANPLSWL WPFSRSPSTE TGLSYEHNEI
DDPSKPWPPP DPDRLFRAER KPLVGDGFTK SWDINDFKER QAADLARYTD GDGEYVVRRR
PFHERLEASR QSERIYEDED AIGTDTESDE EDVRGRPSRR VDEGEEAWRN KEGERLADFG
VDEVADFYDE DDVPLAELIR RRQLAWDRGL ASASASHHRW PSRSSRNSST CLLTIGIITL
LSRRGHAQNS PKMAENVPPN SAQSATAAAD QPGRPYYESL RSTLRQTLDK KRKMDEQLAA
LEENIYKTEG AYLEETANSG NIVRGFDGWV KGVQIGTRSA VDGSRRGGRV REEDRVFSRS
SVSWMRLQEG PDSGTPSHAP TPTGQFPPQL SARDSNASTP AAGSGKAQGN KKKRPTDKDD
EDDLKPSKRH KITYSRE
//
